Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P46821

- MAP1B_HUMAN

UniProt

P46821 - MAP1B_HUMAN

Protein

Microtubule-associated protein 1B

Gene

MAP1B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 2 (11 Jan 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Facilitates tyrosination of alpha-tubulin in neuronal microtubules By similarity. Phosphorylated MAP1B may play a role in the cytoskeletal changes that accompany neurite extension. Possibly MAP1B binds to at least two tubulin subunits in the polymer, and this bridging of subunits might be involved in nucleating microtubule polymerization and in stabilizing microtubules. Acts as a positive cofactor in DAPK1-mediated autophagic vesicle formation and membrane blebbing.By similarity1 Publication

    GO - Molecular functioni

    1. hydrolase activity Source: InterPro
    2. protein binding Source: UniProtKB
    3. structural molecule activity Source: ProtInc

    GO - Biological processi

    1. axon extension Source: Ensembl
    2. cellular process Source: DFLAT
    3. dendrite development Source: Ensembl
    4. establishment of monopolar cell polarity Source: Ensembl
    5. microtubule bundle formation Source: Ensembl
    6. mitochondrion transport along microtubule Source: Ensembl
    7. negative regulation of intracellular transport Source: Ensembl
    8. positive regulation of axon extension Source: Ensembl

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Microtubule-associated protein 1B
    Short name:
    MAP-1B
    Cleaved into the following 2 chains:
    Gene namesi
    Name:MAP1B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:6836. MAP1B.

    Subcellular locationi

    Cytoplasmcytoskeleton 1 Publication. Cytoplasm 1 Publication. Cell junctionsynapse By similarity. Cell projectiondendritic spine By similarity
    Note: Colocalizes with DAPK1 in the microtubules and cortical actin fibers.By similarity

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. cytoplasm Source: HPA
    3. cytosol Source: Ensembl
    4. dendritic spine Source: UniProtKB-SubCell
    5. microtubule Source: UniProtKB-KW
    6. microtubule associated complex Source: ProtInc
    7. plasma membrane Source: DFLAT
    8. synapse Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell projection, Cytoplasm, Cytoskeleton, Microtubule, Synapse

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30581.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 24682467Microtubule-associated protein 1BPRO_0000018604Add
    BLAST
    Chaini2 – 22062205MAP1B heavy chainPRO_0000418379Add
    BLAST
    Chaini2207 – 2468262MAP1 light chain LC1PRO_0000018605Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei336 – 3361Phosphoserine1 Publication
    Modified residuei541 – 5411PhosphoserineBy similarity
    Modified residuei544 – 5441PhosphoserineBy similarity
    Modified residuei561 – 5611PhosphoserineBy similarity
    Modified residuei614 – 6141PhosphoserineBy similarity
    Modified residuei828 – 8281Phosphoserine1 Publication
    Modified residuei831 – 8311Phosphoserine2 Publications
    Modified residuei832 – 8321Phosphoserine2 Publications
    Modified residuei937 – 9371Phosphoserine1 Publication
    Modified residuei992 – 9921Phosphoserine2 Publications
    Modified residuei995 – 9951Phosphoserine2 Publications
    Modified residuei1016 – 10161Phosphoserine3 Publications
    Modified residuei1144 – 11441Phosphoserine1 Publication
    Modified residuei1154 – 11541Phosphoserine1 Publication
    Modified residuei1156 – 11561Phosphoserine1 Publication
    Modified residuei1208 – 12081Phosphoserine1 Publication
    Modified residuei1252 – 12521Phosphoserine1 Publication
    Modified residuei1256 – 12561Phosphoserine1 Publication
    Modified residuei1260 – 12601Phosphoserine1 Publication
    Modified residuei1265 – 12651Phosphoserine2 Publications
    Modified residuei1276 – 12761Phosphoserine1 Publication
    Modified residuei1280 – 12801Phosphoserine1 Publication
    Modified residuei1282 – 12821Phosphothreonine2 Publications
    Modified residuei1312 – 13121PhosphoserineBy similarity
    Modified residuei1378 – 13781Phosphoserine1 Publication
    Modified residuei1387 – 13871Phosphoserine1 Publication
    Modified residuei1389 – 13891Phosphoserine1 Publication
    Modified residuei1396 – 13961Phosphoserine2 Publications
    Modified residuei1400 – 14001Phosphoserine3 Publications
    Modified residuei1427 – 14271Phosphoserine3 Publications
    Modified residuei1438 – 14381Phosphoserine2 Publications
    Modified residuei1443 – 14431Phosphoserine2 Publications
    Modified residuei1501 – 15011Phosphoserine2 Publications
    Modified residuei1618 – 16181Phosphoserine1 Publication
    Modified residuei1620 – 16201Phosphoserine1 Publication
    Modified residuei1625 – 16251Phosphoserine1 Publication
    Modified residuei1653 – 16531Phosphoserine1 Publication
    Modified residuei1779 – 17791Phosphoserine3 Publications
    Modified residuei1782 – 17821Phosphoserine2 Publications
    Modified residuei1785 – 17851Phosphoserine1 Publication
    Modified residuei1788 – 17881Phosphothreonine2 Publications
    Modified residuei1797 – 17971Phosphoserine1 Publication
    Modified residuei1915 – 19151Phosphoserine1 Publication
    Modified residuei1917 – 19171Phosphoserine1 Publication
    Modified residuei1965 – 19651Phosphoserine1 Publication
    Modified residuei2271 – 22711Phosphoserine1 Publication
    Modified residuei2289 – 22891Phosphoserine1 Publication
    Modified residuei2464 – 24641S-nitrosocysteineBy similarity

    Post-translational modificationi

    LC1 is generated from MAP1B by proteolytic processing.1 Publication
    S-nitrosylation at Cys-2464 enhances interaction with microtubules, and may act as an effector modification for neuronal nitric oxide synthase control of growth-cone size, growth-cone collapse and axon retraction.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein, S-nitrosylation

    Proteomic databases

    MaxQBiP46821.
    PaxDbiP46821.
    PRIDEiP46821.

    PTM databases

    PhosphoSiteiP46821.

    Expressioni

    Gene expression databases

    ArrayExpressiP46821.
    BgeeiP46821.
    CleanExiHS_MAP1B.
    GenevestigatoriP46821.

    Organism-specific databases

    HPAiCAB009792.
    HPA022275.

    Interactioni

    Subunit structurei

    3 different light chains, LC1, LC2 and LC3, can associate with MAP1A and MAP1B proteins. LC1 interacts with the amino-terminal region of MAP1B. Interacts with ANP32A and TIAM2. Interacts with the tubulin tyrosine TTL By similarity. Interacts (via C-terminus) with GAN (via Kelch domains). Interacts (via N-terminus) with DAPK1. Interacts with TMEM185A. Interacts with MAP1LC3B.By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GANQ9H2C03EBI-764611,EBI-764342
    LRRK2Q5S0075EBI-9517186,EBI-5323863
    TP53P046376EBI-764611,EBI-366083

    Protein-protein interaction databases

    BioGridi110304. 41 interactions.
    DIPiDIP-33474N.
    IntActiP46821. 28 interactions.
    MINTiMINT-243072.
    STRINGi9606.ENSP00000296755.

    Structurei

    3D structure databases

    ProteinModelPortaliP46821.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati1878 – 189417MAP1B 1Add
    BLAST
    Repeati1895 – 191117MAP1B 2Add
    BLAST
    Repeati1912 – 192817MAP1B 3Add
    BLAST
    Repeati1929 – 194517MAP1B 4Add
    BLAST
    Repeati1946 – 196217MAP1B 5Add
    BLAST
    Repeati1963 – 197917MAP1B 6Add
    BLAST
    Repeati1997 – 201317MAP1B 7Add
    BLAST
    Repeati2014 – 203017MAP1B 8Add
    BLAST
    Repeati2031 – 204717MAP1B 9Add
    BLAST
    Repeati2048 – 206417MAP1B 10Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2294 – 2468175Mediates interaction with TMEM185AAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi589 – 790202Lys-rich (highly basic, contains many KKEE and KKEI/V repeats)Add
    BLAST

    Domaini

    Has a highly basic region with many copies of the sequence KKEE and KKEI/V, repeated but not at fixed intervals, which is responsible for the binding of MAP1B to microtubules.

    Sequence similaritiesi

    Belongs to the MAP1 family.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG12793.
    HOGENOMiHOG000063256.
    HOVERGENiHBG052409.
    InParanoidiP46821.
    KOiK10429.
    OMAiRTPVQDH.
    OrthoDBiEOG773XKP.
    PhylomeDBiP46821.
    TreeFamiTF350229.

    Family and domain databases

    Gene3Di3.60.15.10. 2 hits.
    InterProiIPR001279. Beta-lactamas-like.
    IPR026074. MAP1.
    IPR027321. MAP1B.
    IPR000102. MAP1B_neuraxin.
    [Graphical view]
    PANTHERiPTHR13843. PTHR13843. 1 hit.
    PTHR13843:SF5. PTHR13843:SF5. 1 hit.
    PfamiPF00414. MAP1B_neuraxin. 5 hits.
    [Graphical view]
    PROSITEiPS00230. MAP1B_NEURAXIN. 6 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P46821-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATVVVEATE PEPSGSIANP AASTSPSLSH RFLDSKFYLL VVVGEIVTEE     50
    HLRRAIGNIE LGIRSWDTNL IECNLDQELK LFVSRHSARF SPEVPGQKIL 100
    HHRSDVLETV VLINPSDEAV STEVRLMITD AARHKLLVLT GQCFENTGEL 150
    ILQSGSFSFQ NFIEIFTDQE IGELLSTTHP ANKASLTLFC PEEGDWKNSN 200
    LDRHNLQDFI NIKLNSASIL PEMEGLSEFT EYLSESVEVP SPFDILEPPT 250
    SGGFLKLSKP CCYIFPGGRG DSALFAVNGF NMLINGGSER KSCFWKLIRH 300
    LDRVDSILLT HIGDDNLPGI NSMLQRKIAE LEEEQSQGST TNSDWMKNLI 350
    SPDLGVVFLN VPENLKNPEP NIKMKRSIEE ACFTLQYLNK LSMKPEPLFR 400
    SVGNTIDPVI LFQKMGVGKL EMYVLNPVKS SKEMQYFMQQ WTGTNKDKAE 450
    FILPNGQEVD LPISYLTSVS SLIVWHPANP AEKIIRVLFP GNSTQYNILE 500
    GLEKLKHLDF LKQPLATQKD LTGQVPTPVV KQTKLKQRAD SRESLKPAAK 550
    PLPSKSVRKE SKEETPEVTK VNHVEKPPKV ESKEKVMVKK DKPIKTETKP 600
    SVTEKEVPSK EEPSPVKAEV AEKQATDVKP KAAKEKTVKK ETKVKPEDKK 650
    EEKEKPKKEV AKKEDKTPIK KEEKPKKEEV KKEVKKEIKK EEKKEPKKEV 700
    KKETPPKEVK KEVKKEEKKE VKKEEKEPKK EIKKLPKDAK KSSTPLSEAK 750
    KPAALKPKVP KKEESVKKDS VAAGKPKEKG KIKVIKKEGK AAEAVAAAVG 800
    TGATTAAVMA AAGIAAIGPA KELEAERSLM SSPEDLTKDF EELKAEEVDV 850
    TKDIKPQLEL IEDEEKLKET EPVEAYVIQK EREVTKGPAE SPDEGITTTE 900
    GEGECEQTPE ELEPVEKQGV DDIEKFEDEG AGFEESSETG DYEEKAETEE 950
    AEEPEEDGEE HVCVSASKHS PTEDEESAKA EADAYIREKR ESVASGDDRA 1000
    EEDMDEAIEK GEAEQSEEEA DEEDKAEDAR EEEYEPEKME AEDYVMAVVD 1050
    KAAEAGGAEE QYGFLTTPTK QLGAQSPGRE PASSIHDETL PGGSESEATA 1100
    SDEENREDQP EEFTATSGYT QSTIEISSEP TPMDEMSTPR DVMSDETNNE 1150
    ETESPSQEFV NITKYESSLY SQEYSKPADV TPLNGFSEGS KTDATDGKDY 1200
    NASASTISPP SSMEEDKFSR SALRDAYCSE VKASTTLDIK DSISAVSSEK 1250
    VSPSKSPSLS PSPPSPLEKT PLGERSVNFS LTPNEIKVSA EAEVAPVSPE 1300
    VTQEVVEEHC ASPEDKTLEV VSPSQSVTGS AGHTPYYQSP TDEKSSHLPT 1350
    EVIEKPPAVP VSFEFSDAKD ENERASVSPM DEPVPDSESP IEKVLSPLRS 1400
    PPLIGSESAY ESFLSADDKA SGRGAESPFE EKSGKQGSPD QVSPVSEMTS 1450
    TSLYQDKQEG KSTDFAPIKE DFGQEKKTDD VEAMSSQPAL ALDERKLGDV 1500
    SPTQIDVSQF GSFKEDTKMS ISEGTVSDKS ATPVDEGVAE DTYSHMEGVA 1550
    SVSTASVATS SFPEPTTDDV SPSLHAEVGS PHSTEVDDSL SVSVVQTPTT 1600
    FQETEMSPSK EECPRPMSIS PPDFSPKTAK SRTPVQDHRS EQSSMSIEFG 1650
    QESPEQSLAM DFSRQSPDHP TVGAGVLHIT ENGPTEVDYS PSDMQDSSLS 1700
    HKIPPMEEPS YTQDNDLSEL ISVSQVEASP STSSAHTPSQ IASPLQEDTL 1750
    SDVAPPRDMS LYASLTSEKV QSLEGEKLSP KSDISPLTPR ESSPLYSPTF 1800
    SDSTSAVKEK TATCHSSSSP PIDAASAEPY GFRASVLFDT MQHHLALNRD 1850
    LSTPGLEKDS GGKTPGDFSY AYQKPEETTR SPDEEDYDYE SYEKTTRTSD 1900
    VGGYYYEKIE RTTKSPSDSG YSYETIGKTT KTPEDGDYSY EIIEKTTRTP 1950
    EEGGYSYDIS EKTTSPPEVS GYSYEKTERS RRLLDDISNG YDDSEDGGHT 2000
    LGDPSYSYET TEKITSFPES EGYSYETSTK TTRTPDTSTY CYETAEKITR 2050
    TPQASTYSYE TSDLCYTAEK KSPSEARQDV DLCLVSSCEY KHPKTELSPS 2100
    FINPNPLEWF ASEEPTEESE KPLTQSGGAP PPPGGKQQGR QCDETPPTSV 2150
    SESAPSQTDS DVPPETEECP SITADANIDS EDESETIPTD KTVTYKHMDP 2200
    PPAPVQDRSP SPRHPDVSMV DPEALAIEQN LGKALKKDLK EKTKTKKPGT 2250
    KTKSSSPVKK SDGKSKPLAA SPKPAGLKES SDKVSRVASP KKKESVEKAA 2300
    KPTTTPEVKA ARGEEKDKET KNAANASASK SAKTATAGPG TTKTTKSSAV 2350
    PPGLPVYLDL CYIPNHSNSK NVDVEFFKRV RSSYYVVSGN DPAAEEPSRA 2400
    VLDALLEGKA QWGSNMQVTL IPTHDSEVMR EWYQETHEKQ QDLNIMVLAS 2450
    SSTVVMQDES FPACKIEL 2468
    Length:2,468
    Mass (Da):270,634
    Last modified:January 11, 2011 - v2
    Checksum:i3FFDCB2E20049A8A
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti326 – 3261R → Q in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036016
    Natural varianti574 – 5741V → M in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036017
    Natural varianti594 – 5941I → V.3 Publications
    Corresponds to variant rs1866374 [ dbSNP | Ensembl ].
    VAR_024530
    Natural varianti869 – 8691E → G.
    Corresponds to variant rs16876070 [ dbSNP | Ensembl ].
    VAR_030347
    Natural varianti1296 – 12961P → L.
    Corresponds to variant rs34093016 [ dbSNP | Ensembl ].
    VAR_034105
    Natural varianti1917 – 19171S → R.
    Corresponds to variant rs13153166 [ dbSNP | Ensembl ].
    VAR_056123

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L06237 mRNA. Translation: AAA18904.1.
    BN001084 mRNA. Translation: CAM06633.1.
    AC012609 Genomic DNA. No translation available.
    AC093218 Genomic DNA. No translation available.
    CH471084 Genomic DNA. Translation: EAW95697.1.
    CCDSiCCDS4012.1.
    RefSeqiNP_005900.2. NM_005909.3.
    UniGeneiHs.335079.

    Genome annotation databases

    EnsembliENST00000296755; ENSP00000296755; ENSG00000131711.
    GeneIDi4131.
    KEGGihsa:4131.
    UCSCiuc003kbw.4. human.

    Polymorphism databases

    DMDMi317373388.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L06237 mRNA. Translation: AAA18904.1 .
    BN001084 mRNA. Translation: CAM06633.1 .
    AC012609 Genomic DNA. No translation available.
    AC093218 Genomic DNA. No translation available.
    CH471084 Genomic DNA. Translation: EAW95697.1 .
    CCDSi CCDS4012.1.
    RefSeqi NP_005900.2. NM_005909.3.
    UniGenei Hs.335079.

    3D structure databases

    ProteinModelPortali P46821.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110304. 41 interactions.
    DIPi DIP-33474N.
    IntActi P46821. 28 interactions.
    MINTi MINT-243072.
    STRINGi 9606.ENSP00000296755.

    PTM databases

    PhosphoSitei P46821.

    Polymorphism databases

    DMDMi 317373388.

    Proteomic databases

    MaxQBi P46821.
    PaxDbi P46821.
    PRIDEi P46821.

    Protocols and materials databases

    DNASUi 4131.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000296755 ; ENSP00000296755 ; ENSG00000131711 .
    GeneIDi 4131.
    KEGGi hsa:4131.
    UCSCi uc003kbw.4. human.

    Organism-specific databases

    CTDi 4131.
    GeneCardsi GC05P071438.
    HGNCi HGNC:6836. MAP1B.
    HPAi CAB009792.
    HPA022275.
    MIMi 157129. gene.
    neXtProti NX_P46821.
    PharmGKBi PA30581.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOGENOMi HOG000063256.
    HOVERGENi HBG052409.
    InParanoidi P46821.
    KOi K10429.
    OMAi RTPVQDH.
    OrthoDBi EOG773XKP.
    PhylomeDBi P46821.
    TreeFami TF350229.

    Miscellaneous databases

    ChiTaRSi MAP1B. human.
    GeneWikii MAP1B.
    GenomeRNAii 4131.
    NextBioi 16218.
    PROi P46821.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P46821.
    Bgeei P46821.
    CleanExi HS_MAP1B.
    Genevestigatori P46821.

    Family and domain databases

    Gene3Di 3.60.15.10. 2 hits.
    InterProi IPR001279. Beta-lactamas-like.
    IPR026074. MAP1.
    IPR027321. MAP1B.
    IPR000102. MAP1B_neuraxin.
    [Graphical view ]
    PANTHERi PTHR13843. PTHR13843. 1 hit.
    PTHR13843:SF5. PTHR13843:SF5. 1 hit.
    Pfami PF00414. MAP1B_neuraxin. 5 hits.
    [Graphical view ]
    PROSITEi PS00230. MAP1B_NEURAXIN. 6 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of human microtubule-associated protein 1B and the identification of a related gene on chromosome 15."
      Lien L.L., Feener C., Fischbach N., Kunkel L.M.
      Genomics 22:273-280(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-594.
      Tissue: Fetal brain.
    2. "Hmob3 brain-specific sequence is a part of phylogenetically conserved human MAP1B gene 3'-untranslated region."
      Dergunova L.V., Raevskaya N.M., Vladychenskaya I.P., Limborska S.A.
      Biomol. Eng. 20:91-96(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-594.
    3. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT VAL-594.
    5. Bienvenut W.V., Pchelintsev N., Adams P.D.
      Submitted (OCT-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-31; 55-64; 90-98; 391-429; 520-531; 1052-1070; 1233-1250; 1276-1287; 1462-1476; 1834-1958 AND 1898-1908, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Lung fibroblast.
    6. Lubec G., Afjehi-Sadat L., Vishwanath V., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2347-2370 AND 2382-2409, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    7. "Microtubule-associated protein 1B: a neuronal binding partner for gigaxonin."
      Ding J., Liu J.-J., Kowal A.S., Nardine T., Bhattacharya P., Lee A., Yang Y.
      J. Cell Biol. 158:427-433(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GAN.
    8. "Cloning of a novel neuronally expressed orphan G-protein-coupled receptor which is up-regulated by erythropoietin, interacts with microtubule-associated protein 1b and colocalizes with the 5-hydroxytryptamine 2a receptor."
      Maurer M.H., Gruenewald S., Gassler N., Rossner M., Propst F., Wuerz R., Weber D., Kuner T., Kuschinsky W., Schneider A.
      J. Neurochem. 91:1007-1017(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TMEM185A.
    9. "Gigaxonin-controlled degradation of MAP1B light chain is critical to neuronal survival."
      Allen E., Ding J., Wang W., Pramanik S., Chou J., Yau V., Yang Y.
      Nature 438:224-228(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GAN.
    10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-992; SER-995; SER-1016; SER-1265; SER-1276; SER-1280; THR-1282; SER-1396; SER-1400; SER-1427; SER-1438; SER-1443; SER-1618; SER-1620; SER-1625; SER-1779; SER-1782 AND THR-1788, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
      Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
      Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Prostate cancer.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-336, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    13. "MAP1 structural organization in Drosophila: in vivo analysis of FUTSCH reveals heavy- and light-chain subunits generated by proteolytic processing at a conserved cleavage site."
      Zou B., Yan H., Kawasaki F., Ordway R.W.
      Biochem. J. 414:63-71(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE SITE.
    14. "DAPK-1 binding to a linear peptide motif in MAP1B stimulates autophagy and membrane blebbing."
      Harrison B., Kraus M., Burch L., Stevens C., Craig A., Gordon-Weeks P., Hupp T.R.
      J. Biol. Chem. 283:9999-10014(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DAPK1.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1427, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1016, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    18. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1779, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-831; SER-832; SER-1396; SER-1400 AND SER-1501, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-828; SER-831; SER-832; SER-937; SER-992; SER-995; SER-1016; SER-1144; SER-1154; SER-1156; SER-1208; SER-1252; SER-1256; SER-1260; SER-1265; THR-1282; SER-1378; SER-1387; SER-1389; SER-1400; SER-1427; SER-1438; SER-1443; SER-1501; SER-1653; SER-1779; SER-1782; SER-1785; THR-1788; SER-1797; SER-1915; SER-1917; SER-1965; SER-2271 AND SER-2289, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "Autophagy promotes primary ciliogenesis by removing OFD1 from centriolar satellites."
      Tang Z., Lin M.G., Stowe T.R., Chen S., Zhu M., Stearns T., Franco B., Zhong Q.
      Nature 502:254-257(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAP1LC3B.
    24. Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLN-326 AND MET-574.

    Entry informationi

    Entry nameiMAP1B_HUMAN
    AccessioniPrimary (citable) accession number: P46821
    Secondary accession number(s): A2BDK5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 134 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3